FAM134C Blocking Peptide
- Known as:
- FAM134C Blocking Peptide
- Catalog number:
- 33r-2250
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- FAM134C Blocking Peptide
Related genes to: FAM134C Blocking Peptide
- Gene:
- RETREG3 NIH gene
- Name:
- reticulophagy regulator family member 3
- Previous symbol:
- FAM134C
- Synonyms:
- DKFZp686B1036, FLJ33806
- Chromosome:
- 17q21.2
- Locus Type:
- gene with protein product
- Date approved:
- 2007-05-01
- Date modifiied:
- 2017-03-16
Related products to: FAM134C Blocking Peptide
Related articles to: FAM134C Blocking Peptide
- FAM134/RETREG family members are ER-phagy receptors that maintain cellular homeostasis by regulating endoplasmic reticulum turnover. However, possible non-ER-phagy functions of FAM134 proteins remain elusive. Here, we show that RETREG3/FAM134C functions as a selective autophagy receptor for the type I BMP receptor (BMPRIA/ALK3) and recruits BMPRIA into LC3-containing autophagosomes for subsequent degradation. FAM134C-induced degradation diminishes the availability of BMP receptors and thus the strength of BMP signaling. Inhibition of autophagy through chemical means or knockdown of key autophagy regulators, ATG5 or Beclin-1, prevents BMPR1A degradation. Additionally, disruption of the putative LC3-interacting region (LIR) motif in FAM134C completely abolishes its interaction with LC3, thereby impeding its ability to degrade BMPR1A. Moreover, FAM134C-deficient mice exhibit enhanced BMP responses in the intestines, which affects intestinal crypt regeneration. Our findings suggest that FAM134C acts as a specific receptor that controls BMP signaling through the autophagic degradation of the type I BMP receptor, independent of its canonical role in ER-phagy. - Source: PubMed
Publication date: 2025/10/20
Gu ShuchenZhang HanchenxiCao JinHe ZhouWu JianfengLiu XiaZheng MingjieLiu TingZhao BinXu PinglongSun QimingJin JianpingLin XiaYu YiHan JiahuaiFeng Xin-Hua - Selective macroautophagy/autophagy of the endoplasmic reticulum, known as reticulophagy/ER-phagy, is essential to maintain ER homeostasis. We recently showed that members of the autophagy receptor family RETREG/FAM134 are regulated by phosphorylation-dependent ubiquitination. In an unbiased screen we had identified several kinases downstream of MTOR with profound impact on reticulophagy flux, including ATR and CSNK2/CK2. Inhibition of CSNK2 by SGC-CK2-1 prevented regulatory ubiquitination of RETREG1/FAM134B and RETREG3/FAM134C upon autophagy activation as well as the formation of high-density RETREG1- and RETREG3-clusters. Here we report on additional resource data of global proteomics upon CSNK2 and ATR inhibition, respectively. Our data suggests that the function of CSNK2 is mainly limited to the ER/reticulophagy and Golgi/Golgiphagy, while ATR inhibition by VE-822 affects the vast majority of organelles/selective autophagy pathways. ATRi: ATR inhibitor VE-822; CSNK2i: CSNK2 inhibitor SGC-CK2-1; ER: endoplasmic reticulum. - Source: PubMed
Publication date: 2024/09/03
Sanz-Martinez PabloBerkane RayeneStolz Alexandra - Tuning and assimilation of endoplasmic reticulum (ER) content in each cell of the human body is an essential part of organismal homeostasis and adaptation to stress. As such, the lysosomal turnover of ER (reticulophagy) needs to be regulated in a spatio-temporal as well as cell-type specific manner. We recently identified CSNK2/CK2 (casein kinase 2) as the enzyme that phosphorylates the reticulophagy receptors RETREG1/FAM134B and RETREG3/FAM134C and regulates their activity. Phosphorylation of the receptors is a prerequisite for their subsequent functional ubiquitination and the formation of high-density clusters, presumably representing active macroautophagy/autophagy sites at the ER membrane. Consistently, treatment with kinase inhibitor SGC-CK2-1, knockdown of endogenous CSNK2, or mutation of respective phospho-sites prevents ubiquitination, the formation of high-density clusters as well as reticulophagy flux. We hypothesize that CSNK2 has a broader impact on ER and Golgi content in a cell-type and context-specific manner by orchestrating the activity of several autophagy receptors and potentially also factors of the ER-associated protein degradation pathway. - Source: PubMed
Publication date: 2024/03/21
Stolz Alexandra - Starvation is the most potent physiological inducer of autophagy, the catabolic process which degrades unessential cytosolic components to sustain cellular homeostasis and survival. During starvation, the mechanisms of autophagy activation have been extensively investigated; however, less is known about how substrate selection occurs. In this punctum, we summarize our recent findings that delineate a novel signaling pathway that promotes selective autophagic removal of parts of the endoplasmic reticulum (reticulophagy) during starvation. We demonstrate that the inhibition of MTORC1 results in the activation of the reticulophagy receptor RETREG3/FAM134C by preventing its phosphorylation by CSNK2/CK2. , RETREG3 depletion impairs MTORC1-dependent regulation of lipid metabolism in liver. Last, we describe a novel approach to study selective autophagy , which might be exploited to identify novel physiological roles of autophagy. - Source: PubMed
Publication date: 2022/10/06
Di Lorenzo GiorgiaIavarone FrancescopaoloMaddaluno MariannaGrumati PaoloSettembre Carmine - Degradation of the endoplasmic reticulum (ER) via selective autophagy (ER-phagy) is vital for cellular homeostasis. We identify FAM134A/RETREG2 and FAM134C/RETREG3 as ER-phagy receptors, which predominantly exist in an inactive state under basal conditions. Upon autophagy induction and ER stress signal, they can induce significant ER fragmentation and subsequent lysosomal degradation. FAM134A, FAM134B/RETREG1, and FAM134C are essential for maintaining ER morphology in a LC3-interacting region (LIR)-dependent manner. Overexpression of any FAM134 paralogue has the capacity to significantly augment the general ER-phagy flux upon starvation or ER-stress. Global proteomic analysis of FAM134 overexpressing and knockout cell lines reveals several protein clusters that are distinctly regulated by each of the FAM134 paralogues as well as a cluster of commonly regulated ER-resident proteins. Utilizing pro-Collagen I, as a shared ER-phagy substrate, we observe that FAM134A acts in a LIR-independent manner and compensates for the loss of FAM134B and FAM134C, respectively. FAM134C instead is unable to compensate for the loss of its paralogues. Taken together, our data show that FAM134 paralogues contribute to common and unique ER-phagy pathways. - Source: PubMed
Publication date: 2021/08/02
Reggio AlessioBuonomo VivianaBerkane RayeneBhaskara Ramachandra MTellechea MarianaPeluso IvanaPolishchuk ElenaDi Lorenzo GiorgiaCirillo CarmineEsposito MariannaHussain AdeelaHuebner Antje KHübner Christian ASettembre CarmineHummer GerhardGrumati PaoloStolz Alexandra